Recombinant Human VCAM-1-Fc Chimera (carrier-free)
Description
VCAM-1, vascular cell adhesion molecule 1, is a member of the immunoglobulin superfamily. It is expressed on both large and small blood vessels only after the endothelial cells are stimulated by cytokines, such as IL-4, TNF-α, and IL-1. Within the Ig superfamily, VCAM-1 belongs to a subfamily of cell surface molecules including ICAM-1, -2, and -3, and MAdCAM-1, that bind leukocyte integrin ligands. Members of this family are distinguished by the presence of four cysteine residues instead of the usual two in domains important for counter-receptor binding. Structurally, VCAM-1 exists in two alternatively spliced forms on endothelial cells, a major form comprised of seven Ig-like domains, and a minor form with six Ig-like domains. It has been further demonstrated that domains 1 and 4 of VCAM-1 are critical for binding to its counter-receptor VLA-4 (very late antigen 4, α4β1), while domains 1-3 are important for cell adhesion and costimulation of T cells. The interaction of VCAM-1 and VLA-4 appears to play a role in a number of developmental pathways and inflammatory functions. In addition, it was shown that by interacting with VLA-4, VCAM-1 recruits monocytic osteoclast progenitors and elevates local osteoclast activity. Antibodies against VCAM-1 and integrin α4 effectively inhibit bone metastasis progression and preserve bone structure. These findings establish VCAM-1 as a promising target for the prevention and inhibition of metastatic recurrence in bone.